Date published: 2025-9-16

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C1orf149 Activators

Akt Activators are a diverse array of chemical compounds that indirectly promote the functional activity of the protein Akt through modulation of various cellular signaling pathways. Forskolin, by elevating cAMP levels, indirectly stimulates Akt through PKA activation, which can phosphorylate regulatory proteins that might affect Akt signaling positively. Ionomycin increases intracellular calcium, which could trigger the activation of calcium-dependent protein kinases, facilitating the activation of Akt or related pathways. The PI3K inhibitor LY294002 might enhance Akt activity by disrupting negative feedback loops, while U0126, a MEK inhibitor, could favor Akt activation by reducing competitive MAPK/ERK signaling. Sunitinib's inhibition of tyrosine kinases may allow for enhanced Akt activity by mitigating negative regulatory effects from these pathways. Additionally, the modulation of cellular redox states by N-acetylcysteine could create conditions favoring Akt activation.

Other chemicals contribute to the indirect activation of Akt through metabolic modifications and alterations in gene expression. AICAR, an AMPK activator, induces metabolic shifts that can impact Akt, with AMPK's influence on mTOR signaling potentially facilitating Akt activation. Rosiglitazone, as a PPARγ agonist, may enhance Akt activity by modulating related gene expression networks. Epigallocatechin gallate's kinase-inhibiting properties may reduce competitive signaling, leading to an indirect increase in Akt activation. PMA's activation of PKC, along with SB203580's inhibition of p38 MAPK, can alter signaling pathways intersecting with Akt, which may enhance its activation. Furthermore, TrichostatinA, as a histone deacetylase inhibitor, may influence the expression of proteins that regulate Akt, thus potentially impacting Akt's activation indirectly. Collectively, these chemical activators, through their targeted effects on various signaling pathways and cellular processes, support the enhancement of Akt-mediated functions, demonstrating the complex interplay of intracellular signaling and its influence on Akt activity.

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